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HS71B_PIG
ID   HS71B_PIG               Reviewed;         641 AA.
AC   Q6S4N2;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Heat shock 70 kDa protein 1B;
DE   AltName: Full=Heat shock 70 kDa protein 2;
DE            Short=HSP70.2;
GN   Name=HSPA1B;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen M.Y., Lee W.C.;
RT   "Porcine heat shock protein 70.2 gene.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone implicated in a wide variety of cellular
CC       processes, including protection of the proteome from stress, folding
CC       and transport of newly synthesized polypeptides, activation of
CC       proteolysis of misfolded proteins and the formation and dissociation of
CC       protein complexes. Plays a pivotal role in the protein quality control
CC       system, ensuring the correct folding of proteins, the re-folding of
CC       misfolded proteins and controlling the targeting of proteins for
CC       subsequent degradation. This is achieved through cycles of ATP binding,
CC       ATP hydrolysis and ADP release, mediated by co-chaperones. The co-
CC       chaperones have been shown to not only regulate different steps of the
CC       ATPase cycle, but they also have an individual specificity such that
CC       one co-chaperone may promote folding of a substrate while another may
CC       promote degradation. The affinity for polypeptides is regulated by its
CC       nucleotide bound state. In the ATP-bound form, it has a low affinity
CC       for substrate proteins. However, upon hydrolysis of the ATP to ADP, it
CC       undergoes a conformational change that increases its affinity for
CC       substrate proteins. It goes through repeated cycles of ATP hydrolysis
CC       and nucleotide exchange, which permits cycles of substrate binding and
CC       release. The co-chaperones are of three types: J-domain co-chaperones
CC       such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide
CC       exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70
CC       from the ADP-bound to the ATP-bound state thereby promoting substrate
CC       release), and the TPR domain chaperones such as HOPX and STUB1.
CC       Maintains protein homeostasis during cellular stress through two
CC       opposing mechanisms: protein refolding and degradation. Its
CC       acetylation/deacetylation state determines whether it functions in
CC       protein refolding or protein degradation by controlling the competitive
CC       binding of co-chaperones HOPX and STUB1. During the early stress
CC       response, the acetylated form binds to HOPX which assists in chaperone-
CC       mediated protein refolding, thereafter, it is deacetylated and binds to
CC       ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein
CC       degradation. Regulates centrosome integrity during mitosis, and is
CC       required for the maintenance of a functional mitotic centrosome that
CC       supports the assembly of a bipolar mitotic spindle. Enhances STUB1-
CC       mediated SMAD3 ubiquitination and degradation and facilitates STUB1-
CC       mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated
CC       ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg)
CC       during inflammation. {ECO:0000250|UniProtKB:P0DMV9}.
CC   -!- SUBUNIT: May be an auxiliary component of the CatSper complex.
CC       Identified in a IGF2BP1-dependent mRNP granule complex containing
CC       untranslated mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and
CC       TSC2. Interacts with TERT; the interaction occurs in the absence of the
CC       RNA component, TERC, and dissociates once the TERT complex has formed.
CC       Interacts with METTL21A. Interacts with TRIM5 (via B30.2/SPRY domain).
CC       Interacts with PRKN. Interacts with FOXP3. Interacts with NOD2; the
CC       interaction enhances NOD2 stability. Interacts with DNAJC9 (via J
CC       domain). Interacts with ATF5; the interaction protects ATF5 from
CC       degradation via proteasome-dependent and caspase-dependent processes.
CC       Interacts with NAA10, HSP40, HSP90 and HDAC4. The acetylated form and
CC       the non-acetylated form interact with HOPX and STUB1 respectively.
CC       Interacts with NEDD1 and SMAD3. Interacts (via NBD) with BAG1, BAG2,
CC       BAG3 and HSPH1/HSP105. Interacts with DNAJC8.
CC       {ECO:0000250|UniProtKB:P0DMV9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0DMV9}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P0DMV9}. Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P0DMV9}.
CC   -!- TISSUE SPECIFICITY: Testis-specific.
CC   -!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as
CC       the ATPase domain) is responsible for binding and hydrolyzing ATP. The
CC       C-terminal substrate-binding domain (SBD) (also known as peptide-
CC       binding domain) binds to the client/substrate proteins. The two domains
CC       are allosterically coupled so that, when ATP is bound to the NBD, the
CC       SBD binds relatively weakly to clients. When ADP is bound in the NBD, a
CC       conformational change enhances the affinity of the SBD for client
CC       proteins. {ECO:0000250|UniProtKB:P0DMV9}.
CC   -!- PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and
CC       then gradually deacetylated by HDAC4 at later stages. Acetylation
CC       enhances its chaperone activity and also determines whether it will
CC       function as a chaperone for protein refolding or degradation by
CC       controlling its binding to co-chaperones HOPX and STUB1. The acetylated
CC       form and the non-acetylated form bind to HOPX and STUB1 respectively.
CC       Acetylation also protects cells against various types of cellular
CC       stress. {ECO:0000250|UniProtKB:P0DMV9}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AY466608; AAR30953.1; -; mRNA.
DR   RefSeq; NP_998931.1; NM_213766.1.
DR   AlphaFoldDB; Q6S4N2; -.
DR   SMR; Q6S4N2; -.
DR   PaxDb; Q6S4N2; -.
DR   PeptideAtlas; Q6S4N2; -.
DR   PRIDE; Q6S4N2; -.
DR   Ensembl; ENSSSCT00005066003; ENSSSCP00005040864; ENSSSCG00005041223.
DR   GeneID; 396648; -.
DR   KEGG; ssc:396648; -.
DR   CTD; 100535101; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   InParanoid; Q6S4N2; -.
DR   OrthoDB; 288077at2759; -.
DR   PRO; PR:Q6S4N2; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0090063; P:positive regulation of microtubule nucleation; ISS:UniProtKB.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; ISS:UniProtKB.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   CHAIN           2..641
FT                   /note="Heat shock 70 kDa protein 1B"
FT                   /id="PRO_0000078253"
FT   REGION          2..386
FT                   /note="Nucleotide-binding domain (NBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   REGION          394..509
FT                   /note="Substrate-binding domain (SBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   REGION          617..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         12..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         202..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         268..275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         339..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         77
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         108
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         246
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         348
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         469
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         561
FT                   /note="N6,N6,N6-trimethyllysine; by METTL21A; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         561
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         631
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         633
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
FT   MOD_RES         636
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DMV9"
SQ   SEQUENCE   641 AA;  70098 MW;  9B49BFB380AF0E2A CRC64;
     MAKSVAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
     LNPQNTVFDA KRLIGRKFGD PVVQADMKHW PFRVINDGDK PKVQVSYKGE TKAFYPEEIS
     SMVLTKMKEI AEAYLGHPVS NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
     IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH
     FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
     RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
     KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
     PTKQTQIFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
     DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE IQRERVSAKN
     ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
     QVCNPIISGL YQGAGGPGAG GFGAQAPKGG SGSGPTIEEV D
 
 
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